Acta crystallographica. Section F, Structural biology communications最新文献

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Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis. 重新审视磷钨酸钠和钼酸铵作为用于单颗粒分析的非放射性阴性染色剂。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-12-01 DOI: 10.1107/S2053230X24011294
Monika Gunkel, Arthur Macha, Elmar Behrmann
{"title":"Revisiting sodium phosphotungstate and ammonium molybdate as nonradioactive negative-staining agents for single-particle analysis.","authors":"Monika Gunkel, Arthur Macha, Elmar Behrmann","doi":"10.1107/S2053230X24011294","DOIUrl":"10.1107/S2053230X24011294","url":null,"abstract":"<p><p>This study reports the successful replacement of uranyl-based stains by either sodium phosphotungstate or ammonium molybdate in negative-staining electron microscopy. Using apoferritin as a test specimen, it is demonstrated that in combination with a facile on-grid fixation step, both stains yield comparable images to uranyl formate. Subsequently, using β-galactosidase, it is shown that both stains can also successfully be employed for single-particle analysis, yielding virtually indistinguishable results from uranyl formate. As both replacement stains are nonradioactive, they are not subjected to the same handling restrictions as uranyl-based stains. Therefore they are not only cheaper to use, but also make decentralized sample-grid preparation, directly after purification, accessible to a broader range of scientists.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11614109/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142724691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori. 幽门螺旋杆菌谷氨酰-tRNA 合成酶的晶体结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-12-01 DOI: 10.1107/S2053230X24011099
Dylan E Davis, Jesuferanmi P Ayanlade, David T Laseinde, Sandhya Subramanian, Hannah Udell, Donald J Lorimer, David M Dranow, Thomas E Edwards, Peter J Myler, Oluwatoyin A Asojo
{"title":"Crystal structure of glutamyl-tRNA synthetase from Helicobacter pylori.","authors":"Dylan E Davis, Jesuferanmi P Ayanlade, David T Laseinde, Sandhya Subramanian, Hannah Udell, Donald J Lorimer, David M Dranow, Thomas E Edwards, Peter J Myler, Oluwatoyin A Asojo","doi":"10.1107/S2053230X24011099","DOIUrl":"10.1107/S2053230X24011099","url":null,"abstract":"<p><p>Helicobacter pylori is one of the most common bacterial infections; over two-thirds of the world's population is infected by early childhood. Persistent H. pylori infection results in gastric ulcers and cancers. Due to drug resistance, there is a need to develop alternative treatments to clear H. pylori. The Seattle Structural Genomics Center for Infectious Disease (SSGCID) conducts structure-function analysis of potential therapeutic targets from H. pylori. Glutamyl-tRNA synthetase (GluRS) is essential for tRNA aminoacylation and is under investigation as a bacterial drug target. The SSGCID produced, crystallized and determined the apo structure of H. pylori GluRS (HpGluRS). HpGluRS has the prototypical bacterial GluRS topology and has similar binding sites and tertiary structures to other bacterial GluRS that are promising drug targets. Residues involved in glutamate binding are well conserved in comparison with Pseudomonas aeruginosa GluRS (PaGluRS), which has been studied to develop promising new inhibitors for P. aeruginosa. These structural similarities can be exploited for drug discovery and repurposing to generate new antibacterials to clear persistent H. pylori infection and reduce gastric ulcers and cancer.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11614106/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142724739","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Crystal structure of N-terminally hexahistidine-tagged Onchocerca volvulus macrophage migration inhibitory factor-1. N-末端六脒标记的盘尾丝虫巨噬细胞迁移抑制因子-1的晶体结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-12-01 DOI: 10.1107/S2053230X24010550
Amber D Kimble, Omolara C O Dawson, Lijun Liu, Sandhya Subramanian, Anne Cooper, Kevin Battaile, Justin Craig, Elizabeth Harmon, Peter Myler, Scott Lovell, Oluwatoyin A Asojo
{"title":"Crystal structure of N-terminally hexahistidine-tagged Onchocerca volvulus macrophage migration inhibitory factor-1.","authors":"Amber D Kimble, Omolara C O Dawson, Lijun Liu, Sandhya Subramanian, Anne Cooper, Kevin Battaile, Justin Craig, Elizabeth Harmon, Peter Myler, Scott Lovell, Oluwatoyin A Asojo","doi":"10.1107/S2053230X24010550","DOIUrl":"10.1107/S2053230X24010550","url":null,"abstract":"<p><p>Onchocerca volvulus causes blindness, onchocerciasis, skin infections and devastating neurological diseases such as nodding syndrome. New treatments are needed because the currently used drug, ivermectin, is contraindicated in pregnant women and those co-infected with Loa loa. The Seattle Structural Genomics Center for Infectious Disease (SSGCID) produced, crystallized and determined the apo structure of N-terminally hexahistidine-tagged O. volvulus macrophage migration inhibitory factor-1 (His-OvMIF-1). OvMIF-1 is a possible drug target. His-OvMIF-1 has a unique jellyfish-like structure with a prototypical macrophage migration inhibitory factor (MIF) trimer as the `head' and a unique C-terminal `tail'. Deleting the N-terminal tag reveals an OvMIF-1 structure with a larger cavity than that observed in human MIF that can be targeted for drug repurposing and discovery. Removal of the tag will be necessary to determine the actual biological oligomer of OvMIF-1 because size-exclusion chomatographic analysis of His-OvMIF-1 suggests a monomer, while PISA analysis suggests a hexamer stabilized by the unique C-terminal tails.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11614107/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142581845","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Structures of Trichomonas vaginalis macrophage migratory inhibitory factor. 阴道毛滴虫巨噬细胞迁移抑制因子的结构。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-12-01 DOI: 10.1107/S2053230X24011105
Aruesha Srivastava, Aryana Nair, Omolara C O Dawson, Raymond Gao, Lijun Liu, Justin K Craig, Kevin P Battaile, Elizabeth K Harmon, Lynn K Barrett, Wesley C Van Voorhis, Sandhya Subramanian, Peter J Myler, Scott Lovell, Oluwatoyin A Asojo, Rabih Darwiche
{"title":"Structures of Trichomonas vaginalis macrophage migratory inhibitory factor.","authors":"Aruesha Srivastava, Aryana Nair, Omolara C O Dawson, Raymond Gao, Lijun Liu, Justin K Craig, Kevin P Battaile, Elizabeth K Harmon, Lynn K Barrett, Wesley C Van Voorhis, Sandhya Subramanian, Peter J Myler, Scott Lovell, Oluwatoyin A Asojo, Rabih Darwiche","doi":"10.1107/S2053230X24011105","DOIUrl":"10.1107/S2053230X24011105","url":null,"abstract":"<p><p>The unicellular parasitic protozoan Trichomonas vaginalis causes trichomoniasis, the most prevalent nonviral sexually transmitted disease globally. T. vaginalis evades host immune responses by producing homologs of host proteins, including cytokines such as macrophage migration inhibitory factor. T. vaginalis macrophage migration inhibitory factor (TvMIF) helps to facilitate the survival of T. vaginalis during nutritional stress conditions, increases prostate cell proliferation and invasiveness, and induces inflammation-related cellular pathways, thus mimicking the ability of human MIF to increase inflammation and cell proliferation. The production, crystallization and three structures of N-terminally hexahistidine-tagged TvMIF reveal a prototypical MIF trimer with a topology similar to that of human homologs (hMIF-1 and hMIF-2). The N-terminal tag obscures the expected pyruvate-binding site. The similarity of TvMIF to its human homologs can be exploited for structure-based drug discovery.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":" ","pages":""},"PeriodicalIF":1.1,"publicationDate":"2024-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11614108/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142724696","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
IF 1.1 4区 生物学
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 12","pages":"328-334"},"PeriodicalIF":1.1,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762670","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
IF 1.1 4区 生物学
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 12","pages":"341-347"},"PeriodicalIF":1.1,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762672","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
IF 1.1 4区 生物学
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 12","pages":"356-362"},"PeriodicalIF":1.1,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762669","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
IF 1.1 4区 生物学
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 12","pages":"335-340"},"PeriodicalIF":1.1,"publicationDate":"2024-11-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142762671","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
IF 1.1 4区 生物学
{"title":"","authors":"","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 11","pages":"320-327"},"PeriodicalIF":1.1,"publicationDate":"2024-11-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142579668","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
Multi-species cryoEM calibration and workflow verification standard. 多物种冷冻电镜校准和工作流程验证标准。
IF 1.1 4区 生物学
Acta crystallographica. Section F, Structural biology communications Pub Date : 2024-11-01 Epub Date: 2024-10-31 DOI: 10.1107/S2053230X24010318
Daija Bobe, Mykhailo Kopylov, Jessalyn Miller, Aaron P Owji, Edward T Eng
{"title":"Multi-species cryoEM calibration and workflow verification standard.","authors":"Daija Bobe, Mykhailo Kopylov, Jessalyn Miller, Aaron P Owji, Edward T Eng","doi":"10.1107/S2053230X24010318","DOIUrl":"10.1107/S2053230X24010318","url":null,"abstract":"<p><p>Cryogenic electron microscopy (cryoEM) is a rapidly growing structural biology modality that has been successful in revealing molecular details of biological systems. However, unlike established biophysical and analytical techniques with calibration standards, cryoEM has lacked comprehensive biological test samples. Here, a cryoEM calibration sample consisting of a mixture of compatible macromolecules is introduced that can not only be used for resolution optimization, but also provides multiple reference points for evaluating instrument performance, data quality and image-processing workflows in a single experiment. This combined test specimen provides researchers with a reference point for validating their cryoEM pipeline, benchmarking their methodologies and testing new algorithms.</p>","PeriodicalId":7029,"journal":{"name":"Acta crystallographica. Section F, Structural biology communications","volume":"80 Pt 11","pages":"320-327"},"PeriodicalIF":1.1,"publicationDate":"2024-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11533365/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"142567186","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
引用次数: 0
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